(Q28217860)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12485997%20AND%20SRC:MED&resulttype=core&format=json

15 December 2019

title

Is protein disulfide isomerase a redox-dependent molecular chaperone? (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12485997%20AND%20SRC:MED&resulttype=core&format=json

15 December 2019

0 references

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12485997%20AND%20SRC:MED&resulttype=core&format=json

15 December 2019

author name string

Richard A Lumb

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12485997%20AND%20SRC:MED&resulttype=core&format=json

15 December 2019

language of work or name

English

0 references

publication date

1 December 2002

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12485997%20AND%20SRC:MED&resulttype=core&format=json

15 December 2019

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12485997%20AND%20SRC:MED&resulttype=core&format=json

15 December 2019

volume

21

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12485997%20AND%20SRC:MED&resulttype=core&format=json

15 December 2019

issue

24

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12485997%20AND%20SRC:MED&resulttype=core&format=json

15 December 2019

page(s)

6763-6770

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12485997%20AND%20SRC:MED&resulttype=core&format=json

Manipulation of oxidative protein folding and PDI redox state in mammalian cells

15 December 2019

cites work

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Hsp47: a molecular chaperone that interacts with and stabilizes correctly-folded procollagen

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Site-directed mutagenesis of human protein disulphide isomerase: effect on the assembly, activity and endoplasmic reticulum retention of human prolyl 4-hydroxylase in Spodoptera frugiperda insect cells

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47.

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Quality control in the endoplasmic reticulum: PDI mediates the ER retention of unassembled procollagen C-propeptides

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Intracellular dissociation and reassembly of prolyl 4-hydroxylase:the alpha-subunits associated with the immunoglobulin-heavy-chain binding protein (BiP) allowing reassembly with the beta-subunit

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Cell-free synthesis and assembly of prolyl 4-hydroxylase: the role of the beta-subunit (PDI) in preventing misfolding and aggregation of the alpha-subunit.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Collagens: molecular biology, diseases, and potentials for therapy

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

The C-propeptide domain of procollagen can be replaced with a transmembrane domain without affecting trimer formation or collagen triple helix folding during biosynthesis

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

The translocation, folding, assembly and redox-dependent degradation of secretory and membrane proteins in semi-permeabilized mammalian cells

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex.

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Preparative in vitro mRNA synthesis using SP6 and T7 RNA polymerases.

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=139105

Protein Disulfide Isomerase Acts as a Redox-Dependent Chaperone to Unfold Cholera Toxin

2 June 2018

1 reference

12 December 2020

Dissociation and reassociation of prolyl 4-hydroxylase subunits after cross-linking of monomers

1 reference

12 December 2020

Protein disulfide isomerase appears necessary to maintain the catalytically active structure of the microsomal triglyceride transfer protein

1 reference

12 December 2020

BiP binds type I procollagen pro alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta

1 reference

12 December 2020

Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme

1 reference

12 December 2020

The role of cysteine residues in the folding and association of the COOH-terminal propeptide of types I and III procollagen

1 reference

12 December 2020

Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds

1 reference

12 December 2020

Protein disulphide isomerase: building bridges in protein folding

1 reference

12 December 2020

Prolyl 4-hydroxylase: defective assembly of alpha-subunit mutants indicates that assembled alpha-subunits are intramolecularly disulfide bonded

1 reference

12 December 2020

Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site

1 reference

12 December 2020

Intracellular retention of procollagen within the endoplasmic reticulum is mediated by prolyl 4-hydroxylase

1 reference

12 December 2020

Interactions between protein disulphide isomerase and peptides

1 reference

12 December 2020

Identifiers

DOI

10.1093/EMBOJ/CDF685

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12485997%20AND%20SRC:MED&resulttype=core&format=json

OpenCitations bibliographic resource ID

15 December 2019

1091944

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12485997%20AND%20SRC:MED&resulttype=core&format=json

15 December 2019

PubMed publication ID

12485997

1 reference